ID R7BS49_9FIRM Unreviewed; 496 AA.
AC R7BS49;
DT 24-JUL-2013, integrated into UniProtKB/TrEMBL.
DT 24-JUL-2013, sequence version 1.
DT 27-MAR-2024, entry version 31.
DE RecName: Full=4-alpha-glucanotransferase {ECO:0000256|ARBA:ARBA00020295, ECO:0000256|RuleBase:RU361207};
DE EC=2.4.1.25 {ECO:0000256|ARBA:ARBA00012560, ECO:0000256|RuleBase:RU361207};
DE AltName: Full=Amylomaltase {ECO:0000256|ARBA:ARBA00031423, ECO:0000256|RuleBase:RU361207};
DE AltName: Full=Disproportionating enzyme {ECO:0000256|ARBA:ARBA00031501, ECO:0000256|RuleBase:RU361207};
GN ORFNames=BN674_00979 {ECO:0000313|EMBL:CDD68307.1};
OS Firmicutes bacterium CAG:475.
OC Bacteria; Bacillota.
OX NCBI_TaxID=1263026 {ECO:0000313|EMBL:CDD68307.1, ECO:0000313|Proteomes:UP000018161};
RN [1] {ECO:0000313|EMBL:CDD68307.1, ECO:0000313|Proteomes:UP000018161}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MGS:475 {ECO:0000313|Proteomes:UP000018161};
RA Nielsen H.B., Almeida M., Juncker A.S., Rasmussen S., Li J., Sunagawa S.,
RA Plichta D., Gautier L., Le Chatelier E., Peletier E., Bonde I., Nielsen T.,
RA Manichanh C., Arumugam M., Batto J., Santos M.B.Q.D., Blom N., Borruel N.,
RA Burgdorf K.S., Boumezbeur F., Casellas F., Dore J., Guarner F., Hansen T.,
RA Hildebrand F., Kaas R.S., Kennedy S., Kristiansen K., Kultima J.R.,
RA Leonard P., Levenez F., Lund O., Moumen B., Le Paslier D., Pons N.,
RA Pedersen O., Prifti E., Qin J., Raes J., Tap J., Tims S., Ussery D.W.,
RA Yamada T., MetaHit consortium, Renault P., Sicheritz-Ponten T., Bork P.,
RA Wang J., Brunak S., Ehrlich S.D.;
RT "Dependencies among metagenomic species, viruses, plasmids and units of
RT genetic variation.";
RL Submitted (NOV-2012) to the EMBL/GenBank/DDBJ databases.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=Transfers a segment of a (1->4)-alpha-D-glucan to a new
CC position in an acceptor, which may be glucose or a (1->4)-alpha-D-
CC glucan.; EC=2.4.1.25; Evidence={ECO:0000256|ARBA:ARBA00000439,
CC ECO:0000256|RuleBase:RU361207};
CC -!- SIMILARITY: Belongs to the disproportionating enzyme family.
CC {ECO:0000256|ARBA:ARBA00005684, ECO:0000256|RuleBase:RU361207}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:CDD68307.1}.
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DR EMBL; CBHN010000010; CDD68307.1; -; Genomic_DNA.
DR AlphaFoldDB; R7BS49; -.
DR Proteomes; UP000018161; Unassembled WGS sequence.
DR GO; GO:0004134; F:4-alpha-glucanotransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0102500; F:beta-maltose 4-alpha-glucanotransferase activity; IEA:UniProtKB-EC.
DR GO; GO:0005975; P:carbohydrate metabolic process; IEA:UniProtKB-KW.
DR Gene3D; 3.20.20.80; Glycosidases; 1.
DR InterPro; IPR003385; Glyco_hydro_77.
DR InterPro; IPR017853; Glycoside_hydrolase_SF.
DR NCBIfam; TIGR00217; malQ; 1.
DR PANTHER; PTHR32438; 4-ALPHA-GLUCANOTRANSFERASE DPE1, CHLOROPLASTIC/AMYLOPLASTIC; 1.
DR PANTHER; PTHR32438:SF5; 4-ALPHA-GLUCANOTRANSFERASE DPE1, CHLOROPLASTIC_AMYLOPLASTIC; 1.
DR Pfam; PF02446; Glyco_hydro_77; 1.
DR SUPFAM; SSF51445; (Trans)glycosidases; 1.
PE 3: Inferred from homology;
KW Carbohydrate metabolism {ECO:0000256|RuleBase:RU361207};
KW Glycosyltransferase {ECO:0000256|RuleBase:RU361207};
KW Reference proteome {ECO:0000313|Proteomes:UP000018161};
KW Transferase {ECO:0000256|RuleBase:RU361207}.
SQ SEQUENCE 496 AA; 57100 MW; AF186336CA049F46 CRC64;
MMTDSFGFKH KSGMLTAVSS LPSEWGIGTF GAPCKRFVDF LSATRTKCWQ ILPLNPTAYG
DSPYQSPASF AGNHYYIDPQ TLFEKGLLDG EDLKSAVHVC DKTDYGWLFE SKTALLKKAY
SRFLPDCEFE TFCKDNAKWL DDYAYFMALK AAFGYKAWNE WEDEFRFYDK AQARKGEFAS
EIAFWKFVQY EFFAEWKDVL NYAHSKNITI VGDMPIYVAY DSADVWSNPS MFLLDEDLNP
TVVAGCPPDA YAEDGQLWGN PVYDYDKMKA DGYEWWIERI EQSFKLYDIL RIDHFRGFAG
YFVIKNGEKT AKDGKWMVGP GKSLFDEVNR RIPGAKIIAE DLGFITDDVR ELLAYCGYPG
MKVLQFAFSN DDNEYLPRTY KDENCVVYTG SHDADCTTSW CKKLKGDTLA RFKKECLRFC
GGANRTYAMI NLAFQSVANL AVVPLQDWLL LINEQGRMNT PSVAQGNWVW RAPSNYDNHE
LIDRIRKTNE RFKREN
//
